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Structure of thermotoga maritima S63A non-processing mutant S- adenosylmethionine decarboxylase

Analyse Structure of thermotoga maritima S63A non-processing mutant S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TMI
Type
protein
Length
234 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
S-adenosylmethionine decarboxylase proenzyme, adometdc, samdc
EC
4.1.1.50
UniProt
Q9WZC3

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BS-adenosylmethionine decarboxylase proenzyme, adometdc, samdc (EC 4.1.1.50)protein11727% helix, 46% strandQ9WZC3

Interfaces

1 interface between chains.

  • A–B · 1608 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 1TMI · Structure of Thermotoga maritima S63A non-processing mutant S-adenosylmethionine… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WZC3 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme… · a predicted model of the same protein · chain A against A, TM-score 0.98

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